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The kinetics of alpha-lactalbumin refolding were studied by the stopped-flow method with the registration of CD and intrinsic fluorescence at several wavelengths. It was shown that the early kinetic intermediate forms during the dead-time of the experiment (20 ms). This intermediate has a considerable amount of secondary structure and unpolar clusters in its molecular structure but has no rigid tertiary structure.
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Gilmanshin et al. (1987) studied this question.
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